Characterization of ß-glycosyl hydrolases from Pyrococcus furiosus

Publisher Summary Enzymes from bacterial and archaeal hyperthermophiles have been studied extensively for their catalytic properties and stability at extremely high temperatures, as well as their biotechnological potential as biocatalysts at elevated temperatures. Considerable attention is to sugar-converting enzymes from heterotrophic hyperthermophilic archaea, mainly in members of the archaeal orders Sulfolobales—that is, Sulfolobus solfataricus and Thermococcales—that is, Pyrococcus furiosus . The chapter gives an overview of methods that have been instrumental in the molecular and biochemical characterization of enzymes from Pyrococcus species that catalyze the hydrolysis of β -linked sugars, the β -glycosylhydrolases ( β GHs). These studies form an essential basis for a next generation of experiments, the engineering of β GHs for optimal exploitation of their potential.